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Database: UniProt
Entry: A0A1G8VYQ1_9SPHI
LinkDB: A0A1G8VYQ1_9SPHI
Original site: A0A1G8VYQ1_9SPHI 
ID   A0A1G8VYQ1_9SPHI        Unreviewed;       468 AA.
AC   A0A1G8VYQ1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Glycogen synthase {ECO:0000256|HAMAP-Rule:MF_00484};
DE            EC=2.4.1.21 {ECO:0000256|HAMAP-Rule:MF_00484};
DE   AltName: Full=Starch [bacterial glycogen] synthase {ECO:0000256|HAMAP-Rule:MF_00484};
GN   Name=glgA {ECO:0000256|HAMAP-Rule:MF_00484};
GN   ORFNames=SAMN04487898_10459 {ECO:0000313|EMBL:SDJ71046.1};
OS   Pedobacter sp. ok626.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1761882 {ECO:0000313|EMBL:SDJ71046.1, ECO:0000313|Proteomes:UP000198594};
RN   [1] {ECO:0000313|EMBL:SDJ71046.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK626 {ECO:0000313|EMBL:SDJ71046.1};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
CC       {ECO:0000256|ARBA:ARBA00002764, ECO:0000256|HAMAP-Rule:MF_00484}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-
CC         alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001478, ECO:0000256|HAMAP-
CC         Rule:MF_00484};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00484}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010281, ECO:0000256|HAMAP-Rule:MF_00484}.
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DR   EMBL; FNEX01000004; SDJ71046.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8VYQ1; -.
DR   STRING; 1761882.SAMN04487898_10459; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000198594; Unassembled WGS sequence.
DR   GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR   GO; GO:0009011; F:starch synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   HAMAP; MF_00484; Glycogen_synth; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR011835; GS/SS.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   NCBIfam; TIGR02095; glgA; 1.
DR   PANTHER; PTHR45825; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   PANTHER; PTHR45825:SF11; STARCH SYNTHASE 1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW   Rule:MF_00484};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00484};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00484}.
FT   DOMAIN          3..232
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          278..410
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   BINDING         15
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   468 AA;  53174 MW;  DD0B5C75E754733E CRC64;
     MEIIHLSAEC YPIAKVGGLG DVVGALPKYQ NKLGHVAKVV MPAYQNKFIQ ENEFEVVYDG
     WGKLGFHNFT VKIFREKTNK LGFDLYLVHI AGLLDREMVY GYDDDTERFL AYQIAVLDWM
     AQWEHRPDVI HCHDHHTGLV PFMVAYCHQF KSLSHIPTVL TIHNAQYQGQ FGWDKLHYIP
     TFDLWKSGQL DWKGAINPLA AAIKCAWRVT TVSPSYLDEI SFKANGLEDL LAQERSKSFG
     ILNGIDNEVW NPQTDPMLEK KFTLRTVDAG KQANKEALCK VFNLDPEKPL FTFIGRLVGE
     KGADLLPDIF YNALITHNGE INVLVLGSGD PQVEGRLWQL KEAFPGNYNV YIGYNEHLSH
     QIYAGADFLL MPSRVEPCGL NQMYALRYGT IPIVRRVGGL KDTVIDIGDG GFGICHDQSS
     VWDVGHAIGR AYDLYQNAKE VKEIRKFIMQ LDHSWDKAAQ QYIDLYQI
//
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